Enzyme Nomenclature

Continued from EC 2.7.7.51 to 2.7.7.103

EC 2.7.8 and EC 2.7.9

Sections

EC 2.7.8 Transferases for other substituted phosphate groups
EC 2.7.9 Phosphotransferases with paired acceptors


EC 2.7.8 Transferases for other substituted phosphate groups

Contents

EC 2.7.8.1 ethanolaminephosphotransferase
EC 2.7.8.2 diacylglycerol cholinephosphotransferase
EC 2.7.8.3 ceramide cholinephosphotransferase
EC 2.7.8.4 serine-phosphoethanolamine synthase
EC 2.7.8.5 CDP-diacylglycerol—glycerol-3-phosphate 1-phosphatidyltransferase
EC 2.7.8.6 undecaprenyl-phosphate galactose phosphotransferase
EC 2.7.8.7 holo-[acyl-carrier-protein] synthase
EC 2.7.8.8 CDP-diacylglycerol—serine O-phosphatidyltransferase
EC 2.7.8.9 phosphomannan mannosephosphotransferase
EC 2.7.8.10 sphingosine cholinephosphotransferase
EC 2.7.8.11 CDP-diacylglycerol—inositol 3-phosphatidyltransferase
EC 2.7.8.12 teichoic acid poly(glycerol phosphate) polymerase
EC 2.7.8.13 phospho-N-acetylmuramoyl-pentapeptide-transferase
EC 2.7.8.14 CDP-ribitol ribitolphosphotransferase
EC 2.7.8.16 deleted, included in EC 2.7.8.2
EC 2.7.8.15 UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase
EC 2.7.8.17 UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase
EC 2.7.8.18 UDP-galactose—UDP-N-acetylglucosamine galactose phosphotransferase
EC 2.7.8.19 UDP-glucose—glycoprotein glucose phosphotransferase
EC 2.7.8.20 phosphatidylglycerol—membrane-oligosaccharide glycerophosphotransferase
EC 2.7.8.21 membrane-oligosaccharide glycerophosphotransferase
EC 2.7.8.22 1-alkenyl-2-acylglycerol choline phosphotransferase
EC 2.7.8.23 carboxyvinyl-carboxyphosphonate phosphorylmutase
EC 2.7.8.24 phosphatidylcholine synthase
EC 2.7.8.25 transferred now EC 2.4.2.52
EC 2.7.8.26 adenosylcobinamide-GDP ribazoletransferase
EC 2.7.8.27 sphingomyelin synthase
EC 2.7.8.28 2-phospho-L-lactate transferase
EC 2.7.8.29 L-serine-phosphatidylethanolamine phosphatidyltransferase
EC 2.7.8.30 transferred now EC 2.4.2.53
EC 2.7.8.31 undecaprenyl-phosphate glucose phosphotransferase
EC 2.7.8.32 3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase
EC 2.7.8.33 UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
EC 2.7.8.34 CDP-L-myo-inositol myo-inositolphosphotransferase
EC 2.7.8.35 UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase
EC 2.7.8.36 undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
EC 2.7.8.37 α-D-ribose 1-methylphosphonate 5-triphosphate synthase
EC 2.7.8.38 archaetidylserine synthase
EC 2.7.8.39 archaetidylinositol phosphate synthase
EC 2.7.8.40 UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase
EC 2.7.8.41 cardiolipin synthase (CMP-forming)
EC 2.7.8.42 Kdo2-lipid A phosphoethanolamine 7''-transferase
EC 2.7.8.43 lipid A phosphoethanolamine transferase
EC 2.7.8.44 teichoic acid glycerol-phosphate primase
EC 2.7.8.45 teichoic acid glycerol-phosphate transferase
EC 2.7.8.46 teichoic acid ribitol-phosphate primase
EC 2.7.8.47 teichoic acid ribitol-phosphate polymerase

Entries

EC 2.7.8.1

Accepted name: ethanolaminephosphotransferase

Reaction: CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine

Other name(s): EPT; diacylglycerol ethanolaminephosphotransferase; CDPethanolamine diglyceride phosphotransferase; phosphorylethanolamine-glyceride transferase; CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase

Systematic name: CDP-ethanolamine:1,2-diacyl-sn-glycerol ethanolaminephosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-19-1

References:

1. Kennedy, E.P. and Weiss, S.B. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222 (1956) 193-214.

[EC 2.7.8.1 created 1961]

EC 2.7.8.2

Accepted name: diacylglycerol cholinephosphotransferase

Reaction: CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine

Other name(s): phosphorylcholine-glyceride transferase; alkylacylglycerol cholinephosphotransferase; 1-alkyl-2-acetylglycerol cholinephosphotransferase; cholinephosphotransferase; CPT; alkylacylglycerol choline phosphotransferase; diacylglycerol choline phosphotransferase; 1-alkyl-2-acetyl-m-glycerol:CDPcholine choline phosphotransferase; CDP-choline diglyceride phosphotransferase; cytidine diphosphocholine glyceride transferase; cytidine diphosphorylcholine diglyceride transferase; phosphocholine diacylglyceroltransferase; sn-1,2-diacylglycerol cholinephosphotransferase; 1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase; CDP choline:1,2-diacylglycerol cholinephosphotransferase; CDP-choline:1,2-diacylglycerol cholinephosphotransferase

Systematic name: CDP-choline:1,2-diacyl-sn-glycerol cholinephosphotransferase

Comments: 1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed as EC 2.7.8.16, 1-alkyl-2-acylglycerol choline phosphotransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-13-5

References:

1. Coleman, R. and Bell, R.M. Phospholipid synthesis in isolated fat cells. Studies of microsomal diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase activities. J. Biol. Chem. 252 (1977) 3050-3056. [PMID: 192727]

2. Lee, T.-C., Blank, M.L., Fitzgerald, V. and Snyder, F. Formation of alkylacyl- and diacylglycerophosphocholines via diradylglycerol cholinephosphotransferase in rat liver. Biochim. Biophys. Acta 713 (1982) 479-483. [PMID: 6295501]

3. Parsasarathy, S., Cady, R.K., Kraushaar, D.S., Sladek, N.E. and Baumann, W.J. Inhibition of diacylglycerol:CDPcholine cholinephosphotransferase activity by dimethylaminoethyl p-chlorophenoxyacetate. Lipids 13 (1978) 161-164. [PMID: 204847]

4. Renooij, W. and Snyder, F. Biosynthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet activating factor and a hypotensive lipid) by cholinephosphotransferase in various rat tissues. Biochim. Biophys. Acta 663 (1981) 545-556. [PMID: 6260215]

[EC 2.7.8.2 created 1961, modified 1986 (EC 2.7.8.16 created 1983, incorporated 1986)]

EC 2.7.8.3

Accepted name: ceramide cholinephosphotransferase

Reaction: CDP-choline + an N-acylsphingosine = CMP + a sphingomyelin

Other names: phosphorylcholine-ceramide transferase

Systematic name: CDP-choline:N-acylsphingosine cholinephosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-14-6

References:

1. Kennedy, E.P. Phosphorylcholine-glyceride transferase. Methods Enzymol. 5 (1962) 484-486.

2. Sribney, M. and Kennedy, E.P. The enzymatic synthesis of sphingomyelin. J. Biol. Chem. 233 (1958) 1315-1322.

[EC 2.7.8.3 created 1965]

EC 2.7.8.4

Accepted name: serine-phosphoethanolamine synthase

Reaction: CDP-ethanolamine + L-serine = CMP + L-serine-phosphoethanolamine

Other names: serine ethanolamine phosphate synthetase; serine ethanolamine phosphodiester synthase; serine ethanolaminephosphotransferase; serine-phosphinico-ethanolamine synthase; serinephosphoethanolamine synthase

Systematic name: CDP-ethanolamine:L-serine ethanolamine phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9023-23-8

References:

1. Allen, A.K. and Rosenberg, H. The mechanism of action and some properties of serine ethanolamine phosphate synthetase. Biochim. Biophys. Acta 151 (1968) 504-519. [PMID: 5636380]

[EC 2.7.8.4 created 1972, modified 1976]

EC 2.7.8.5

Accepted name: CDP-diacylglycerol—glycerol-3-phosphate 1-phosphatidyltransferase

Reaction: CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 1-(3-sn-phosphatidyl)-sn-glycerol 3-phosphate

Other name(s): glycerophosphate phosphatidyltransferase; 3-phosphatidyl-1'-glycerol-3'-phosphate synthase; CDPdiacylglycerol:glycerol-3-phosphate phosphatidyltransferase; cytidine 5'-diphospho-1,2-diacyl-sn-glycerol (CDP-diglyceride):sn-glycerol-3-phosphate phosphatidyltransferase; phosphatidylglycerophosphate synthase; phosphatidylglycerolphosphate synthase; PGP synthase; CDP-diacylglycerol-sn-glycerol-3-phosphate 3-phosphatidyltransferase; CDP-diacylglycerol:sn-glycero-3-phosphate phosphatidyltransferase; glycerol phosphate phosphatidyltransferase; glycerol 3-phosphate phosphatidyltransferase; phosphatidylglycerol phosphate synthase; phosphatidylglycerol phosphate synthetase; phosphatidylglycerophosphate synthetase; sn-glycerol-3-phosphate phosphatidyltransferase

Systematic name: CDP-diacylglycerol:sn-glycerol-3-phosphate 1-(3-sn-phosphatidyl)transferase

Comments: The enzyme catalyses the committed step in the biosynthesis of acidic phospholipids known by the common names phophatidylglycerols and cardiolipins.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-49-9

References:

1. Hirabayashi, T. Larson, T.J. and Dowhan, W. Membrane-associated phosphatidylglycerophosphate synthetase from Escherichia coli: Purification by substrate affinity chromatography on cytidine 5'-diphospho-1,2-diacyl-sn-glycerol sepharose. Biochemistry 15 (1976) 5205-5211. [PMID: 793612]

2. Bleasdale, J.E. and Johnston, J.M. CMP-dependent incorporation of [14C]glycerol 3-phosphate into phosphatidylglycerol and phosphatidylglycerol phosphate by rabbit lung microsomes. Biochim. Biophys. Acta 710 (1982) 377-390. [PMID: 7074121]

3. Dowhan, W. Phosphatidylglycerophosphate synthase from Escherichia coli. Methods Enzymol. 209 (1992) 313-321. [PMID: 1323047]

4. Kawasaki, K., Kuge, O., Chang, S.C., Heacock, P.N., Rho, M., Suzuki, K., Nishijima, M. and Dowhan, W. Isolation of a chinese hamster ovary (CHO) cDNA encoding phosphatidylglycerophosphate (PGP) synthase, expression of which corrects the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-K1 cells. J. Biol. Chem. 274 (1999) 1828-1834. [PMID: 9880566]

5. Muller, F. and Frentzen, M. Phosphatidylglycerophosphate synthases from Arabidopsis thaliana. FEBS Lett. 509 (2001) 298-302. [PMID: 11741606]

6. Babiychuk, E., Muller, F., Eubel, H., Braun, H.P., Frentzen, M. and Kushnir, S. Arabidopsis phosphatidylglycerophosphate synthase 1 is essential for chloroplast differentiation, but is dispensable for mitochondrial function. Plant J. 33 (2003) 899-909. [PMID: 12609031]

[EC 2.7.8.5 created 1972, modified 1976, modified 2016]

EC 2.7.8.6

Accepted name: undecaprenyl-phosphate galactose phosphotransferase

Reaction: UDP-α-D-galactose + undecaprenyl phosphate = UMP + α-D-galactosyl-diphosphoundecaprenol

Other name(s): poly(isoprenol)-phosphate galactose phosphotransferase; poly(isoprenyl)phosphate galactosephosphatetransferase; undecaprenyl phosphate galactosyl-1-phosphate transferase; UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase

Systematic name: UDP-α-D-galactose:undecaprenyl-phosphate galactose phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-29-8

References:

1. Osborn, M.J. and Yuan Tze-Yuen, R. Biosynthesis of bacterial lipopolysaccharide. VII. Enzymatic formation of the first intermediate in biosynthesis of the O-antigen of Salmonella typhimurium. J. Biol. Chem. 243 (1968) 5145-5152. [PMID: 4878433]

2. Wright, A., Dankert, M., Fennessen, P. and Robbins, P.W. Characterization of a polyisoprenoid compound functional in O-antigen biosynthesis. Proc. Natl. Acad. Sci. USA 57 (1967) 1798-1803. [PMID: 4291948]

[EC 2.7.8.6 created 1972]

EC 2.7.8.7

Accepted name: holo-[acyl-carrier-protein] synthase

Reaction: CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]

Other name(s): acyl carrier protein holoprotein (holo-ACP) synthetase; holo-ACP synthetase; coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase; holosynthase; acyl carrier protein synthetase; holo-ACP synthase; PPTase; AcpS; ACPS; acyl carrier protein synthase; P-pant transferase; CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase

Systematic name: CoA-[4'-phosphopantetheine]:apo-[acyl-carrier protein] 4'-pantetheinephosphotransferase

Comments: Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4′-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.

Comments: Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-30-1

References:

1. Elovson, J. and Vagelos, P.R. Acyl carrier protein. X. Acyl carrier protein synthetase. J. Biol. Chem. 243 (1968) 3603-3611. [PMID: 4872726]

2. Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269-311. [PMID: 4561013]

3. Lambalot, R.H., Gehring, A.M., Flugel, R.S., Zuber, P., LaCelle, M., Marahiel, M.A., Reid, R., Khosla, C. and Walsh, C.T. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3 (1996) 923-936. [PMID: 8939709]

4. Walsh, C.T., Gehring, A.M., Weinreb, P.H., Quadri, L.E.N. and Flugel, R.S. Post-translational modification of polyketide and nonribosomal peptide synthases. Curr. Opin. Chem. Biol. 1 (1997) 309-315. [PMID: 9667867]

5. Mootz, H.D., Finking, R. and Marahiel, M.A. 4'-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J. Biol. Chem. 276 (2001) 37289-37298. [PMID: 11489886]

6. Joshi, A.K., Zhang, L., Rangan, V.S. and Smith, S. Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity. J. Biol. Chem. 278 (2003) 33142-33149. [PMID: 12815048]

[EC 2.7.8.7 created 1972, modified 2006]

EC 2.7.8.8

Accepted name: CDP-diacylglycerol—serine O-phosphatidyltransferase

Reaction: CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine

Other name(s): phosphatidylserine synthase; CDPdiglyceride-serine O-phosphatidyltransferase; PS synthase; cytidine 5'-diphospho-1,2-diacyl-sn-glycerol (CDPdiglyceride):L-serine O-phosphatidyltransferase; phosphatidylserine synthetase; CDP-diacylglycerol-L-serine O-phosphatidyltransferase; cytidine diphosphoglyceride-serine O-phosphatidyltransferase; CDP-diglyceride-L-serine phosphatidyltransferase; CDP-diglyceride:serine phosphatidyltransferase; cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine O-phosphatidyltransferase; CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase

Systematic name: CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-48-8

References:

1. Larson, T.J. and Dowhan, W. Ribosomal-associated phosphatidylserine synthetase from Escherichia coli: purification by substrate-specific elution from phosphocellulose using cytidine 5'-diphospho-1,2-diacyl-sn-glycerol. Biochemistry 15 (1976) 5212-5218. [PMID: 187212]

2. Raetz, C.R.H. and Kennedy, E.P. Partial purification and properties of phosphatidylserine synthetase from Escherichia coli. J. Biol. Chem. 249 (1974) 5038-5045. [PMID: 4604873]

[EC 2.7.8.8 created 1972, modified 1976]

EC 2.7.8.9

Accepted name: phosphomannan mannosephosphotransferase

Reaction: GDP-mannose + (phosphomannan)n = GMP + (phosphomannan)n+1

Systematic name: GDP-mannose:phosphomannan mannose phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-31-2

References:

1. Bretthauer, R.K., Kozak, L.P. and Irwin, W.E. Phosphate and mannose transfer from guanosine diphosphate mannose to yeast mannan acceptors. Biochem. Biophys. Res. Commun. 37 (1969) 820-827. [PMID: 4311996]

[EC 2.7.8.9 created 1972]

EC 2.7.8.10

Accepted name: sphingosine cholinephosphotransferase

Reaction: CDP-choline + sphingosine = CMP + sphingosyl-phosphocholine

Other names: CDP-choline-sphingosine cholinephosphotransferase; phosphorylcholine-sphingosine transferase; cytidine diphosphocholine-sphingosine cholinephosphotransferase; sphingosine choline phosphotransferase

Systematic name: CDP-choline:sphingosine cholinephosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-12-7

References:

1. Fujino, Y., Nigishi, T. and Ito, S. Enzymic synthesis of sphingosylphosphorylcholine. Biochem. J. 109 (1968) 310-311. [PMID: 5679375]

[EC 2.7.8.10 created 1972, modified 1976]

EC 2.7.8.11

Accepted name: CDP-diacylglycerol—inositol 3-phosphatidyltransferase

Reaction: CDP-diacylglycerol + myo-inositol = CMP + 1-phosphatidyl-1D-myo-inositol

For diagram click here.

Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns

Other name(s): CDP-diglyceride—inositol phosphatidyltransferase; phosphatidylinositol synthase; CDP-diacylglycerol-inositol phosphatidyltransferase; CDP-diglyceride:inositol transferase; cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:myo-inositol 3-phosphatidyltransferase; CDP-DG:inositol transferase; cytidine diphosphodiglyceride-inositol phosphatidyltransferase; CDP-diacylglycerol:myo-inositol-3-phosphatidyltransferase; CDP-diglyceride-inositol transferase; cytidine diphosphoglyceride-inositol phosphatidyltransferase; cytidine diphosphoglyceride-inositol transferase

Systematic name: CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-01-4

References:

1. Bleasdale, J.E., Wallis, P., MacDonald, P.C. and Johnston, J.M. Characterization of the forward and reverse reactions catalyzed by CDP-diacylglycerol:inositol transferase in rabbit lung tissue. Biochim. Biophys. Acta 575 (1979) 135-147. [PMID: 41587]

2. Prottey, C. and Hawthorne, J.N. The biosynthesis of phosphatidic acid and phosphatidylinositol in mammalian pancreas. Biochem. J. 105 (1967) 379-392. [PMID: 4293959]

3. Salway, J.G., Harewood, J.L., Kai, M., White, G.L. and Hawthorne, J.N. Enzymes of phosphoinositide metabolism during rat brain development. J. Neurochem. 15 (1968) 221-226. [PMID: 4295616]

4. Takenawa, T. and Egawa, K. CDP-diglyceride:inositol transferase from rat liver. Purification and properties. J. Biol. Chem. 252 (1977) 5419-5423. [PMID: 18462]

[EC 2.7.8.11 created 1972, modified 1976]

EC 2.7.8.12

Accepted name: teichoic acid poly(glycerol phosphate) polymerase

Reaction: n CDP-glycerol + 4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): teichoic-acid synthase; cytidine diphosphoglycerol glycerophosphotransferase; poly(glycerol phosphate) polymerase; teichoic acid glycerol transferase; glycerophosphate synthetase; CGPTase; CDP-glycerol glycerophosphotransferase (ambiguous); Tag polymerase; CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase; tagF (gene name); tarF (gene name) (ambiguous)

Systematic name: CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase

Comments: Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30-50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-71-5

References:

1. Burger, M.M. and Glaser, L. The synthesis of teichoic acids. I. Polyglycerophosphate. J. Biol. Chem. 239 (1964) 3168-3177. [PMID: 14245357]

2. Schertzer, J.W. and Brown, E.D. Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro. J. Biol. Chem. 278 (2003) 18002-18007. [PMID: 12637499]

3. Schertzer, J.W., Bhavsar, A.P. and Brown, E.D. Two conserved histidine residues are critical to the function of the TagF-like family of enzymes. J. Biol. Chem. 280 (2005) 36683-36690. [PMID: 16141206]

4. Pereira, M.P., Schertzer, J.W., D'Elia, M.A., Koteva, K.P., Hughes, D.W., Wright, G.D. and Brown, E.D. The wall teichoic acid polymerase TagF efficiently synthesizes poly(glycerol phosphate) on the TagB product lipid III. Chembiochem 9 (2008) 1385-1390. [PMID: 18465758]

5. Sewell, E.W., Pereira, M.P. and Brown, E.D. The wall teichoic acid polymerase TagF is non-processive in vitro and amenable to study using steady state kinetic analysis. J. Biol. Chem. 284 (2009) 21132-21138. [PMID: 19520862]

6. Lovering, A.L., Lin, L.Y., Sewell, E.W., Spreter, T., Brown, E.D. and Strynadka, N.C. Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis. Nat. Struct. Mol. Biol. 17 (2010) 582-589. [PMID: 20400947]

7. Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101-1110. [PMID: 21035733]

[EC 2.7.8.12 created 1972, modified 1982, modified 2017]

EC 2.7.8.13

Accepted name: phospho-N-acetylmuramoyl-pentapeptide-transferase

Reaction: UDP-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

For diagram click here.

Other names: MraY transferase; UDP-MurNAc-L-Ala-D-γ-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase; UDP-MurNAc-Ala-γDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase; phospho-N-acetylmuramoyl pentapeptide translocase; phospho-MurNAc-pentapeptide transferase; phospho-NAc-muramoyl-pentapeptide translocase (UMP); phosphoacetylmuramoylpentapeptide translocase; phosphoacetylmuramoylpentapeptidetransferase

Systematic name: UDP-MurAc(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase

Comments: In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9068-50-2

References:

1. Heydanek, M.G., Jr. and Neuhaus, F.C. The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase. Biochemistry 8 (1969) 1474-1481. [PMID: 5805290]

2. Higashi, Y., Strominger, J.L. and Sweeley, C.C. Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol. Proc. Natl. Acad. Sci. USA 57 (1967) 1878-1884. [PMID: 5231417]

3. Struve, W.G., Sinha, R.K. and Neuhaus, F.C. On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate). Biochemistry 5 (1966) 82-93. [PMID: 5938956]

4. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]

[EC 2.7.8.13 created 1972, modified 2002]

EC 2.7.8.14

Accepted name: CDP-ribitol ribitolphosphotransferase

Reaction: n CDP-ribitol + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): teichoic-acid synthase (ambiguous); polyribitol phosphate synthetase (ambiguous); teichoate synthetase (ambiguous); poly(ribitol phosphate) synthetase (ambiguous); polyribitol phosphate polymerase (ambiguous); teichoate synthase (ambiguous); CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase

Systematic name: CDP-ribitol:4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase

Comments: Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds around 40 ribitol units to the linker molecule.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-71-5

References:

1. Ishimoto, N. and Strominger, J.L. Polyribitol phosphate synthetase of Staphylococcus aureus. J. Biol. Chem. 241 (1966) 639-650. [PMID: 5908130]

2. Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12-21. [PMID: 18215769]

3. Pereira, M.P., D'Elia, M.A., Troczynska, J. and Brown, E.D. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190 (2008) 5642-5649. [PMID: 18556787]

4. Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101-1110. [PMID: 21035733]

[EC 2.7.8.14 created 1972 as EC 2.4.1.55, transferred 1982 to EC 2.7.8.14, modified 2017]

EC 2.7.8.15

Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphosphodolichol

For diagram of reaction click here.

Other name(s): UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase; uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase; chitobiosylpyrophosphoryldolichol synthase; dolichol phosphate N-acetylglucosamine-1-phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase

Systematic name: UDP-N-α-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase (configuration-retaining)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70431-08-2

References:

1. Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319-325. [PMID: 6215245]

2. Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem. 255 (1980) 8174-8178. [PMID: 6447695]

[EC 2.7.8.15 created 1983]

[EC 2.7.8.16 Deleted entry: 1-alkyl-2-acetylglycerol choline phosphotransferase. Now included with EC 2.7.8.2 diacylglycerol cholinephosphotransferase (EC 2.7.8.16 created 1983, deleted 1986)]

EC 2.7.8.17

Accepted name: UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase

Reaction: UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose

Other name(s): N-acetylglucosaminylphosphotransferase; UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-glycoprotein acetylglucosamine-1-phosphotransferase; lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; N-acetylglucosaminyl phosphotransferase; UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminyl-1-phosphotransferase

Systematic name: UDP-N-acetyl-D-glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase

Comments: Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84012-69-1

References:

1. Reitman, M.L. and Kornfeld, S. UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J. Biol. Chem. 256 (1981) 4275-4281. [PMID: 6452459]

2. Reitman, M.L. and Kornfeld, S. Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes. J. Biol. Chem. 256 (1981) 11977-11980. [PMID: 6457829]

3. Waheed, A., Hasilik, A. and von Figura, K. UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme. J. Biol. Chem. 257 (1982) 12322-12331. [PMID: 6288715]

4. Waheed, A., Pohlmann, R., Hasilik, A. and von Figura, K. Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes. J. Biol. Chem. 256 (1981) 4150-4152. [PMID: 6260788]

[EC 2.7.8.17 created 1984]

EC 2.7.8.18

Accepted name: UDP-galactose—UDP-N-acetylglucosamine galactose phosphotransferase

Reaction: UDP-α-D-galactose + UDP-N-acetyl-α-D-glucosamine = UMP + UDP-N-acetyl-6-(α-D-galactose-1-phospho)-α-D-glucosamine

Other names: uridine diphosphogalactose-uridine diphosphoacetylglucosamine galactose-1-phosphotransferase; galactose-1-phosphotransferase; galactosyl phosphotransferase; UDP-galactose:UDP-N-acetyl-D-glucosamine galactose phosphotransferase

Systematic name: UDP-α-D-galactose:UDP-N-acetyl-D-glucosamine galactose phosphotransferase

Comments: N-Acetylglucosamine end-groups in glycoproteins can also act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84932-43-4

References:

1. Nakanishi, Y., Otsu, K. and Suzuki, S. Enzymatic transfer of galactosyl phosphate from UDP-galactose to UDP-N-acetylglucosamine. FEBS Lett. 151 (1983) 15-18. [PMID: 6130977]

[EC 2.7.8.18 created 1986]

EC 2.7.8.19

Accepted name: UDP-glucose—glycoprotein glucose phosphotransferase

Reaction: UDP-glucose + glycoprotein D-mannose = UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose

Other names: UDP-glucose:glycoprotein glucose-1-phosphotransferase; GlcPTase; Glc-phosphotransferase; uridine diphosphoglucose-glycoprotein glucose-1-phosphotransferase

Systematic name: UDP-glucose:glycoprotein-D-mannose glucosephosphotransferase

Comments: Penultimate mannose residues on oligo-mannose type glycoproteins can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84861-40-5

References:

1. Koro, L.A. and Marchase, R.B. A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina. Cell 31 (1982) 739-748. [PMID: 6297779]

[EC 2.7.8.19 created 1986]

EC 2.7.8.20

Accepted name: phosphatidylglycerol—membrane-oligosaccharide glycerophosphotransferase

Reaction: phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose

Other name(s): phosphoglycerol transferase; oligosaccharide glycerophosphotransferase; phosphoglycerol transferase I

Systematic name: phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase

Comments: 1,2-β- and 1,6-β-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80146-86-7

References:

1. Jackson, B.J. and Kennedy, E.P. The biosynthesis of membrane-derived oligosaccharides. A membrane-bound phosphoglycerol transferase. J. Biol. Chem. 258 (1983) 2394-2398. [PMID: 6296144]

[EC 2.7.8.20 created 1986]

EC 2.7.8.21

Accepted name: membrane-oligosaccharide glycerophosphotransferase

Reaction: Transfer of a glycerophospho group from one membrane-derived oligosaccharide to another

Other name(s): periplasmic phosphoglycerotransferase; phosphoglycerol cyclase

Systematic name: membrane-derived-oligosaccharide-6-(glycerophospho)-D-glucose:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase

Comments: β-Linked glucose residues in simple glucosides, such as gentiobiose, can act as acceptors. In the presence of low concentrations of acceptor, free cyclic 1,2-phosphoglycerol is formed.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80146-86-7

References:

1. Goldberg, D.E., Rumley, M.K. and Kennedy, E.P. Biosynthesis of membrane-derived oligosaccharides: a periplasmic phosphoglyceroltransferase. Proc. Natl. Acad. Sci. USA 78 (1981) 5513-5517. [PMID: 6272307]

[EC 2.7.8.21 created 1986]

EC 2.7.8.22

Accepted name: 1-alkenyl-2-acylglycerol choline phosphotransferase

Reaction: CDP-choline + 1-alkenyl-2-acylglycerol = CMP + plasmenylcholine

Other names: CDP-choline-1-alkenyl-2-acyl-glycerol phosphocholinetransferase

Systematic name: CDP-choline:1-alkenyl-2-acylglycerol cholinephosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113066-36-7

References:

1. Wientzek, M., Man, R.Y.K. and Choy, P.C. Choline glycerophospholipid biosynthesis in the guinea pig heart. Biochem. Cell. Biol. 65 (1987) 860-868. [PMID: 3447597]

[EC 2.7.8.22 created 1990]

EC 2.7.8.23

Accepted name: carboxyvinyl-carboxyphosphonate phosphorylmutase

Reaction: 1-carboxyvinyl carboxyphosphonate = 3-(hydrohydroxyphosphoryl)pyruvate + CO2

Systematic name: 1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating)

Comments: catalyses the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 122799-57-9

References:

1. Pollack, S.J., Freeman, S., Pompliano, D.L., Knowles, J.R. Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus. Eur. J. Biochem. 209 (1992) 735-743. [PMID: 1330557]

2. Anzai, H., Murakami, T., Imai, S., Satoh, A., Nagaoka, K., Thompson, C.J. Transcriptional regulation of bialaphos biosynthesis in Streptomyces hygroscopicus. J. Bacteriol. 169 (1987) 3482-3488. [PMID: 3611020]

[EC 2.7.8.23 created 1999]

EC 2.7.8.24

Accepted name: phosphatidylcholine synthase

Reaction: CDP-diacylglycerol + choline = CMP + phosphatidylcholine

Other name(s): CDP-diglyceride-choline O-phosphatidyltransferase

Systematic name: CDP-diacylglycerol:choline O-phosphatidyltransferase

Comments: Requires divalent cations, with Mn2+ being more effective than Mg2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 243666-86-6

References:

1. de Rudder, K.E.E., Sohlenkamp, C. and Geiger, O. Plant-exudated choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase. J. Biol. Chem. 274 (1999) 20011-20016. [PMID: 10391951]

2. Sohlenkamp, C., de Rudder, K.E.E., Röhrs, V., López-Lara, I.M. and Geiger, O. Cloning and characterization of the gene for phosphatidylcholine synthase. J. Biol. Chem. 275 (2000) 18919-18925. [PMID: 10858449]

[EC 2.7.8.24 created 2001]

[EC 2.7.8.25 Transferred entry: triphosphoribosyl-dephospho-CoA synthase. Now EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase (EC 2.7.8.25 created 2002, modified 2008, deleted 2013)]

EC 2.7.8.26

Accepted name: adenosylcobinamide-GDP ribazoletransferase

Reaction: adenosylcobinamide-GDP + α-ribazole = GMP + adenosylcobalamin

For diagram click here.

Other name(s): CobS; cobalamin synthase; cobalamin-5'-phosphate synthase; cobalamin (5'-phosphate) synthase

Systematic name: adenosylcobinamide-GDP:α-ribazole ribazoletransferase

Comments: In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, α-ribazole. The second branch of the nuclotide loop assembly pathway is the cobinamide activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme Cob U. CobS catalyses the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with α-ribazole to yield adenosylcobalamin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 137672-85-6

References:

1. Maggio-Hall, L.A. and Escalante-Semerena, J.C. In vitro synthesis of the nucleotide loop of cobalamin by Salmonella typhimurium enzymes. Proc. Natl. Acad. Sci. USA 96 (1999) 11798-11803. [PMID: 10518530]

2. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]

3. Cameron, B., Blanche, F., Rouyez, M.C., Bisch, D., Famechon, A., Couder, M., Cauchois, L., Thibaut, D., Debussche, L. and Crouzet, J. Genetic analysis, nucleotide sequence, and products of two Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide: dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5'-phosphate) synthase. J. Bacteriol. 173 (1991) 6066-6073. [PMID: 1917841]

[EC 2.7.8.26 created 2004]

EC 2.7.8.27

Accepted name: sphingomyelin synthase

Reaction: a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol

For diagram click here.

Glossary: sphingomyelin = a ceramide-1-phosphocholine
ceramide = an N-acylsphingoid. The fatty acids of naturally occurring ceramides range in chain length from about C16 to about C26 and may contain one or more double bonds and/or hydroxy substituents at C-2
sphingoid = sphinganine, i.e. D-erythro-2-aminooctadecane-1,3-diol, and its homologues and stereoisomers (see also Lip-1.4)

Other name(s): SM synthase; SMS1; SMS2

Systematic name: ceramide:phosphatidylcholine cholinephosphotransferase

Comments: The reaction can occur in both directions [3]. This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism [4]. Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types [4]. Unlike EC 2.7.8.3, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 58703-97-2

References:

1. Ullman, M.D. and Radin, N.S. The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J. Biol. Chem. 249 (1974) 1506-1512. [PMID: 4817756]

2. Voelker, D.R. and Kennedy, E.P. Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21 (1982) 2753-2759. [PMID: 7093220]

3. Huitema, K., van den Dikkenberg, J., Brouwers, J.F. and Holthuis, J.C. Identification of a family of animal sphingomyelin synthases. EMBO J. 23 (2004) 33-44. [PMID: 14685263]

4. Tafesse, F.G., Ternes, P. and Holthuis, J.C. The multigenic sphingomyelin synthase family. J. Biol. Chem. 281 (2006) 29421-29425. [PMID: 16905542]

5. Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H. and Okazaki, T. Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J. Biol. Chem. 279 (2004) 18688-18693. [PMID: 14976195]

[EC 2.7.8.27 created 2006]

EC 2.7.8.28

Accepted name: 2-phospho-L-lactate transferase

Reaction: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + coenzyme F420-0

For diagram of reaction click here.

Glossary: coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
GMP = guanosine 5'-phosphate

Other name(s): LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; MJ1256, lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase; CofD

Systematic name: (2S)-lactyl-2-diphospho-5'-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase

Comments: This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Graupner, M., Xu, H. and White, R.H. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F420 biosynthesis in Methanococcus jannaschii. Biochemistry 41 (2002) 3754-3761. [PMID: 11888293]

2. Forouhar, F., Abashidze, M., Xu, H., Grochowski, L.L., Seetharaman, J., Hussain, M., Kuzin, A., Chen, Y., Zhou, W., Xiao, R., Acton, T.B., Montelione, G.T., Galinier, A., White, R.H. and Tong, L. Molecular insights into the biosynthesis of the F420 coenzyme. J. Biol. Chem. 283 (2008) 11832-11840. [PMID: 18252724]

[EC 2.7.8.28 created 2010]

EC 2.7.8.29

Accepted name: L-serine-phosphatidylethanolamine phosphatidyltransferase

Reaction: L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine

Other name(s): phosphatidylserine synthase 2; serine-exchange enzyme II; PTDSS2 (gene name)

Systematic name: L-1-phosphatidylethanolamine:L-serine phosphatidyltransferase

Comments: This mammalian enzyme catalyses an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Stone, S.J. and Vance, J.E. Cloning and expression of murine liver phosphatidylserine synthase (PSS)-2: differential regulation of phospholipid metabolism by PSS1 and PSS2. Biochem. J. 342 (1999) 57-64. [PMID: 10432300]

2. Tomohiro, S., Kawaguti, A., Kawabe, Y., Kitada, S. and Kuge, O. Purification and characterization of human phosphatidylserine synthases 1 and 2. Biochem. J. 418 (2009) 421-429. [PMID: 19014349]

[EC 2.7.8.29 created 2010]

[EC 2.7.8.30 Transferred entry: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase. Now EC 2.4.2.53, undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (EC 2.7.8.30 created 2010, modified 2011, deleted 2013)]

EC 2.7.8.31

Accepted name: undecaprenyl-phosphate glucose phosphotransferase

Reaction: UDP-glucose + ditrans,octacis-undecaprenyl phosphate = UMP + α-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol

For diagram of the reaction click here.

Other name(s): GumD; undecaprenylphosphate glucosylphosphate transferase

Systematic name: UDP-glucose:-ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase

Comments: The enzyme is involved in biosynthesis of xanthan.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ielpi, L., Couso, R.O. and Dankert, M.A. Sequential assembly and polymerization of the polyprenol-linked pentasaccharide repeating unit of the xanthan polysaccharide in Xanthomonas campestris. J. Bacteriol. 175 (1993) 2490-2500. [PMID: 7683019]

2. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]

3. Kim, S.Y., Kim, J.G., Lee, B.M. and Cho, J.Y. Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae. Biotechnol. Lett. 31 (2009) 265-270. [PMID: 18854951]

[EC 2.7.8.31 created 2011]

EC 2.7.8.32

Accepted name: 3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase

Reaction: UDP-xylose + 3-O-α-D-mannopyranosyl-α-D-mannopyranose = UMP + 3-O-(6-O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose

Glossary: O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose = O-α-D-xylosylphosphono-α-D-mannopyranosyl)-α-D-mannopyranose

Other name(s): XPT1

Systematic name: UDP-D-xylose:3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase

Comments: Mn2+ required for activity. The enzyme is specific for mannose as an acceptor but is flexible as to the structural context of the mannosyl disaccharide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Reilly, M.C., Levery, S.B., Castle, S.A., Klutts, J.S. and Doering, T.L. A novel xylosylphosphotransferase activity discovered in Cryptococcus neoformans. J. Biol. Chem. 284 (2009) 36118-36127. [PMID: 19864415]

[EC 2.7.8.32 created 2011]

EC 2.7.8.33

Accepted name: UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate

Other name(s): UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase; UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase; GlcNAc-P-P-Und synthase; GPT (ambiguous)s; TagO; UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-D-glucosaminephosphotransferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-α-D-glucosaminephosphotransferase

Comments: This enzyme catalyses the synthesis of ditrans,octacis-undecaprenyl-N-acetyl-D-glucosaminyl diphosphate, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J. Bacteriol. 190 (2008) 7141-7146. [PMID: 18723618]

2. Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide. J. Bacteriol. 189 (2007) 2618-2628. [PMID: 17237164]

4. Soldo, B., Lazarevic, V. and Karamata, D. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 (2002) 2079-2087. [PMID: 12101296]

[EC 2.7.8.33 created 2011]

EC 2.7.8.34

Accepted name: CDP-L-myo-inositol myo-inositolphosphotransferase

Reaction: CDP-1L-myo-inositol + 1L-myo-inositol 1-phosphate = CMP + bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate

For diagram of reaction click here.

Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate

Other name(s): CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS))

Systematic name: CDP-1L-myo-inositol:1L-myo-inositol 1-phosphate myo-inositolphosphotransferase

Comments: In many organisms this activity is catalysed by a bifunctional enzyme. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405-5412. [PMID: 17526717]

[EC 2.7.8.34 created 2011]

EC 2.7.8.35

Accepted name: UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + trans,octacis-decaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol

For diagram of reaction click here.

Other name(s): GlcNAc-1-phosphate transferase; UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase

Comments: Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-α-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jin, Y., Xin, Y., Zhang, W. and Ma, Y. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol. Lett. 310 (2010) 54-61. [PMID: 20637039]

[EC 2.7.8.35 created 2012]

EC 2.7.8.36

Accepted name: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase

Reaction: UDP-N,N'-diacetylbacillosamine + tritrans,heptacis-undecaprenyl phosphate = UMP + N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol

For diagram of reaction click here.

Glossary: UDP-N,N'-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose

Other name(s): PglC

Systematic name: UDP-N,N'-diacetylbacillosamine:tritrans,heptacis-undecaprenyl-phosphate N,N'-diacetylbacillosamine transferase

Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Glover, K.J., Weerapana, E., Chen, M.M. and Imperiali, B. Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 45 (2006) 5343-5350. [PMID: 16618123]

[EC 2.7.8.36 created 2012]

EC 2.7.8.37

Accepted name: α-D-ribose 1-methylphosphonate 5-triphosphate synthase

Reaction: ATP + methylphosphonate = α-D-ribose 1-methylphosphonate 5-triphosphate + adenine

For diagram of reaction click here.

Systematic name: ATP:methylphosphonate 5-triphosphoribosyltransferase

Comments: Isolated from the bacterium Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570-573. [PMID: 22089136]

[EC 2.7.8.37 created 2012]

EC 2.7.8.38

Accepted name: archaetidylserine synthase

Reaction: (1) CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine
(2) CDP-2,3-bis-(O-phytanyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine

For diagram of reaction click here.

Glossary: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol = CDP-unsaturated archaeol
2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine = unsaturated archaetidylserine
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP archaeol
2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine = archaetidylserine

Systematic name: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol:L-serine 2,3-bis-(O-geranylgeranyl)-sn-glycerol phosphotransferase

Comments: Requires Mn2+. Isolated from the archaeon Methanothermobacter thermautotrophicus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181-1189. [PMID: 12562787]

[EC 2.7.8.38 created 2013, modified 2013]

EC 2.7.8.39

Accepted name: archaetidylinositol phosphate synthase

Reaction: CDP-2,3-bis-(O-phytanyl)-sn-glycerol + 1L-myo-inositol 1-phosphate = CMP + 1-archaetidyl-1D-myo-inositol 3-phosphate

Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP-2,3-di-(O-phytanyl)-sn-glycerol = CDP-archaeol
1-archaetidyl-1D-myo-inositol 3-phosphate = archaetidyl-myo-inositol 1-phosphate

Other name(s): AIP synthase

Systematic name: CDP-2,3-bis-(O-phytanyl)-sn-glycerol:1L-myo-inositol 1-phosphate 1-sn-archaetidyltransferase

Comments: Requires Mg2+ or Mn2+ for activity. The enzyme is involved in biosynthesis of archaetidyl-myo-inositol, a compound essential for glycolipid biosynthesis in archaea.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Morii, H., Kiyonari, S., Ishino, Y. and Koga, Y. A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in methanoarchaeon Methanothermobacter thermautotrophicus cells. J. Biol. Chem. 284 (2009) 30766-30774. [PMID: 19740749]

[EC 2.7.8.39 created 2013]

EC 2.7.8.40

Accepted name: UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): WecP; UDP-GalNAc:polyprenol-P GalNAc-1-P transferase; UDP-GalNAc:undecaprenyl-phosphate GalNAc-1-phosphate transferase

Systematic name: UDP-N-acetyl-α-D-galactosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-D-galactosaminephosphotransferase

Comments: The enzyme catalyses a step in the assembly of the repeating-unit of the O-antigen of the Gram-negative bacterium Aeromonas hydrophila AH-3. The enzyme shows no activity with UDP-N-acetyl-α-D-glucosamine (cf. EC 2.7.8.33, UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Merino, S., Jimenez, N., Molero, R., Bouamama, L., Regue, M. and Tomas, J.M. A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family. J. Bacteriol. 193 (2011) 1943-1952. [PMID: 21335454]

[EC 2.7.8.40 created 2013]

EC 2.7.8.41

Accepted name: cardiolipin synthase (CMP-forming)

Reaction: a CDP-diacylglycerol + a phosphatidylglycerol = a cardiolipin + CMP

Systematic name: CDP-diacylglycerol:phosphatidylglycerol diacylglycerolphosphotransferase (CMP-forming)

Comments: The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin. It requires divalent cations for activity.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Schlame, M. and Hostetler, K.Y. Solubilization, purification, and characterization of cardiolipin synthase from rat liver mitochondria. Demonstration of its phospholipid requirement. J. Biol. Chem. 266 (1991) 22398-22403. [PMID: 1657995]

2. Nowicki, M., Muller, F. and Frentzen, M. Cardiolipin synthase of Arabidopsis thaliana. FEBS Lett 579 (2005) 2161-2165. [PMID: 15811335]

3. Houtkooper, R.H., Akbari, H., van Lenthe, H., Kulik, W., Wanders, R.J., Frentzen, M. and Vaz, F.M. Identification and characterization of human cardiolipin synthase. FEBS Lett 580 (2006) 3059-3064. [PMID: 16678169]

4. Sandoval-Calderon, M., Geiger, O., Guan, Z., Barona-Gomez, F. and Sohlenkamp, C. A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria. J. Biol. Chem. 284 (2009) 17383-17390. [PMID: 19439403]

5. Sarma, P.V., Srikanth, L., Venkatesh, K., Murthy, P.S. and Sarma, P.U. Isolation, purification and characterization of cardiolipin synthase from Mycobacterium phlei. Bioinformation 9 (2013) 690-695. [PMID: 23930021]

[EC 2.7.8.41 created 2014]

EC 2.7.8.42

Accepted name: Kdo2-lipid A phosphoethanolamine 7''-transferase

Reaction: (1) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A
(2) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IVA = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IVA

Glossary: lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s): eptB (gene name)

Systematic name: diacylphosphatidylethanolamine:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A 7''-phosphoethanolaminetransferase

Comments: The enzyme has been characterized from the bacterium Escherichia coli. It is activated by Ca2+ ions and is is silenced by the sRNA MgrR.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kanipes, M.I., Lin, S., Cotter, R.J. and Raetz, C.R. Ca2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli lipopolysaccharide. A novel membrane enzyme dependent upon phosphatidylethanolamine. J. Biol. Chem. 276 (2001) 1156-1163. [PMID: 11042192]

2. Reynolds, C.M., Kalb, S.R., Cotter, R.J. and Raetz, C.R. A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant. J. Biol. Chem. 280 (2005) 21202-21211. [PMID: 15795227]

3. Moon, K., Six, D.A., Lee, H.J., Raetz, C.R. and Gottesman, S. Complex transcriptional and post-transcriptional regulation of an enzyme for lipopolysaccharide modification. Mol. Microbiol. 89 (2013) 52-64. [PMID: 23659637]

[EC 2.7.8.42 created 2015]

EC 2.7.8.43

Accepted name: lipid A phosphoethanolamine transferase

Reaction: (1) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
(2) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
(3) diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate)

Glossary: lipid A (Campylobacter jejuni) = 2,3-dideoxy-2,3-bis[(3R)-3-(hexadecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Escherichia coli) =
2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Helicobacter pylori) = 2-deoxy-2-[(3R)-3-(octadecanoyloxy)octadecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyhexadecanoyl]-2-[(3R)-3-hydroxyoctadecanamido]-α-D-glucopyranosyl phosphate
lipid A (Neisseria meningitidis) =
2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-[(2-aminoethyl) diphosphate] = P1-(2-aminoethyl)
P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate
lipid A 1,4'-bis(2-aminoethyl diphosphate) = P1-(2-aminoethyl)
P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-(2-aminoethyldiphospho)-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate

Other name(s): lipid A PEA transferase; LptA

Systematic name: diacylphosphatidylethanolamine:lipid-A ethanolaminephosphotransferase

Comments: The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-β-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Tran, A.X., Karbarz, M.J., Wang, X., Raetz, C.R., McGrath, S.C., Cotter, R.J. and Trent, M.S. Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A. J. Biol. Chem. 279 (2004) 55780-55791. [PMID: 15489235]

2. Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444-1460. [PMID: 20384697]

3. Cullen, T.W. and Trent, M.S. A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni. Proc. Natl. Acad. Sci. USA 107 (2010) 5160-5165. [PMID: 20194750]

4. Anandan, A., Piek, S., Kahler, C.M. and Vrielink, A. Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1494-1497. [PMID: 23192031]

5. Wanty, C., Anandan, A., Piek, S., Walshe, J., Ganguly, J., Carlson, R.W., Stubbs, K.A., Kahler, C.M. and Vrielink, A. The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin. J. Mol. Biol. 425 (2013) 3389-3402. [PMID: 23810904]

[EC 2.7.8.43 created 2015 as EC 2.7.4.30, transferred 2016 to EC 2.7.8.43]

EC 2.7.8.44

Accepted name: teichoic acid glycerol-phosphate primase

Reaction: CDP-glycerol + N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CDP + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): Tag primase; CDP-glycerol:glycerophosphate glycerophosphotransferase; tagB (gene name); tarB (gene name)

Systematic name: CDP-glycerol:N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase

Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls. This enzyme adds the first glycerol unit to the disaccharide linker of the teichoic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bhavsar, A.P., Truant, R. and Brown, E.D. The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro. J. Biol. Chem. 280 (2005) 36691-36700. [PMID: 16150696]

2. Ginsberg, C., Zhang, Y.H., Yuan, Y. and Walker, S. In vitro reconstitution of two essential steps in wall teichoic acid biosynthesis. ACS Chem. Biol. 1 (2006) 25-28. [PMID: 17163636]

3. Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12-21. [PMID: 18215769]

[EC 2.7.8.44 created 2016]

EC 2.7.8.45

Accepted name: teichoic acid glycerol-phosphate transferase

Reaction: CDP-glycerol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CDP + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): tarF (gene name) (ambiguous); teichoic acid glycerol-phosphate primase

Systematic name: CDP-glycerol:4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase

Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell walls of some bacteria such as Staphylococcus aureus. This enzyme adds a second glycerol unit to the disaccharide linker of the teichoic acid. cf. EC 2.7.8.12, teichoic acid poly(glycerol phosphate) polymerase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12-21. [PMID: 18215769]

2. Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101-1110. [PMID: 21035733]

[EC 2.7.8.45 created 2017]

EC 2.7.8.46

Accepted name: teichoic acid ribitol-phosphate primase

Reaction: CDP-ribitol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CMP + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): Tar primase; tarK (gene name)

Systematic name: CDP-ribitol:4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitylphosphotransferase

Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the first ribitol unit to the disaccharide linker of the teichoic acid.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101-1110. [PMID: 21035733]

[EC 2.7.8.46 created 2017]

EC 2.7.8.47

Accepted name: teichoic acid ribitol-phosphate polymerase

Reaction: n CDP-ribitol + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-[(1-D-ribitylphospho)n-(1-D-ribitylphospho)-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): Tar polymerase (ambiguous); tarL (gene name) (ambiguous)

Systematic name: CDP-ribitol:4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase

Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the 25-35 ribitol units to the linker molecule.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101-1110. [PMID: 21035733]

[EC 2.7.8.47 created 2017]


EC 2.7.9 Phosphotransferases with paired acceptors

Contents

EC 2.7.9.1 pyruvate, phosphate dikinase
EC 2.7.9.2 pyruvate, water dikinase
EC 2.7.9.3 selenide, water dikinase
EC 2.7.9.4 α-glucan, water dikinase
EC 2.7.9.5 phosphoglucan, water dikinase
EC 2.7.9.6 rifampicin phosphotransferase


Entries

EC 2.7.9.1

Accepted name: pyruvate, phosphate dikinase

Reaction: ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate

Other names: pyruvate, orthophosphate dikinase; pyruvate-phosphate dikinase (phosphorylating); pyruvate, phosphate dikinase; pyruvate-inorganic phosphate dikinase; pyruvate-phosphate dikinase; pyruvate-phosphate ligase; pyruvic-phosphate dikinase; pyruvic-phosphate ligase; pyruvate, Pi dikinase; PPDK

Systematic name: ATP:pyruvate, phosphate phosphotransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-40-1

References:

1. Hatch, M.D. and Slack, C.R. A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role in the C4 dicarboxylic acid pathway of photosynthesis. Biochem. J. 106 (1968) 141-146. [PMID: 4305612]

2. Reeves, R.E. A new enzyme with the glycolytic function of pyruvate kinase. J. Biol. Chem. 243 (1968) 3202-3204. [PMID: 4297474]

3. Reeves, R.E. Pyruvate, phosphate dikinase from Bacteroides symbiosus. Biochem. J. 125 (1971) 531-539. [PMID: 5144757]

4. Reeves, R.E., Menzies, R.A. and Hsu, D.S. The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium. J. Biol. Chem. 243 (1968) 5486-5491. [PMID: 4302788]

[EC 2.7.9.1 created 1972]

EC 2.7.9.2

Accepted name: pyruvate, water dikinase

Reaction: ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate

For diagram of reaction click here.

Other name(s): phosphoenolpyruvate synthase; pyruvate-water dikinase (phosphorylating); PEP synthetase; phosphoenolpyruvate synthase; phoephoenolpyruvate synthetase; phosphoenolpyruvic synthase; phosphopyruvate synthetase

Systematic name: ATP:pyruvate, water phosphotransferase

Comments: A manganese protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-09-6

References:

1. Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions. J. Biol. Chem. 245 (1970) 5309-5318 [PMID: 4319237]

2. Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H218O exchange reaction. J. Biol. Chem. 245 (1970) 5319-5325. [PMID: 4319238]

3. Cooper, R.A. and Kornberg, H.L. Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli. Biochim. Biophys. Acta 104 (1965) 618-620. [PMID: 5322808]

4. Cooper, R.A. and Kornberg, H.L. Phosphoenolpyruvate synthetase. Methods Enzymol. 13 (1969) 309-314.

[EC 2.7.9.2 created 1976]

EC 2.7.9.3

Accepted name: selenide, water dikinase

Reaction: ATP + selenide + H2O = AMP + selenophosphate + phosphate

Other name(s): selenophosphate synthase

Systematic name: ATP:selenide, water phosphotransferase

Comments: Mg2+-dependent enzyme identified in Escherichia coli

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 151125-25-6

References:

1. Veres, Z., Tsai, L., Scholz, T.D., Politino, M., Balaban, R.S., Stadtman, T.C. Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesised by the selD gene product contains selenium bonded to phosphorus. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 2975-2979. [PMID: 1557403]

[EC 2.7.9.3 created 1999]

EC 2.7.9.4

Accepted name: α-glucan, water dikinase

Reaction: ATP + α-glucan + H2O = AMP + phospho-α-glucan + phosphate

Other name(s): starch-related R1 protein, GWD

Systematic name: ATP:α-glucan, water phosphotransferase

Comments: Requires Mg2+. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate [1]. The protein phosphorylates glucans exclusively at the O-6 position of glucosyl residues [2]. The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 664327-94-0

References:

1. Ritte, G., Lloyd, J.R., Eckermann, N., Rottmann, A., Kossmann, J. and Steup, M. The starch-related R1 protein is an α-glucan, water dikinase. Proc. Natl. Acad. Sci. USA 99 (2002) 7166-7171. [PMID: 12011472]

2. Ritte, G., Heydenreich, M., Mahlow, S., Haebel, S., Kötting, O. and Steup, M. Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases. FEBS Lett. 580 (2006) 4872-4876. [PMID: 16914145]

[EC 2.7.9.4 created 2002]

EC 2.7.9.5

Accepted name: phosphoglucan, water dikinase

Reaction: ATP + [phospho-α-glucan] + H2O = AMP + O-phospho-[phospho-α-glucan] + phosphate

Other name(s): PWD; OK1

Systematic name: ATP:phospho-α-glucan, water phosphotransferase

Comments: The enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, α-glucan, water dikinase; there is no activity with unphosphorylated glucans. It transfers the β-phosphate of ATP to the phosphoglucan, whereas the γ-phosphate is transferred to water [1]. In contrast to EC 2.7.9.4, which phosphorylates the glucose groups in glucans predominantly on the O-6 position, this enzyme phosphorylates glucose groups in phosphorylated starch predominantly on O-3 [2]. The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 912567-76-1

References:

1. Kötting, O., Pusch, K., Tiessen, A., Geigenberger, P., Steup, M. and Ritte, G. Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase. Plant Physiol. 137 (2005) 242-252. [PMID: 15618411]

2. Ritte, G., Heydenreich, M., Mahlow, S., Haebel, S., Kötting, O. and Steup, M. Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases. FEBS Lett. 580 (2006) 4872-4876. [PMID: 16914145]

[EC 2.7.9.5 created 2005]

EC 2.7.9.6

Accepted name: rifampicin phosphotransferase

Reaction: ATP + rifampicin + H2O = AMP + 21-phosphorifampicin + phosphate

For diagram of reaction click here.

Glossary: rifampicin = rifampin = 3-[(4-methylpiperazin-1-yl)iminomethyl]rifamycin

Other name(s): rifampin phosphotransferase; RPH

Systematic name: ATP:rifampicin, water 21-O-phosphotransferase

Comments: The enzyme, characterized from a diverse collection of Gram-positive bacteria, inactivates the antibiotic rifampicin by phosphorylating it at position 21. The enzyme comprises three domains: two substrate-binding domains (ATP-grasp and rifampicin-binding domains) and a smaller phosphate-carrying L-histidine swivel domain that transits between the spatially distinct substrate-binding sites during catalysis.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Spanogiannopoulos, P., Waglechner, N., Koteva, K. and Wright, G.D. A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria. Proc. Natl Acad. Sci. USA 111 (2014) 7102-7107. [PMID: 24778229]

2. Stogios, P.J., Cox, G., Spanogiannopoulos, P., Pillon, M.C., Waglechner, N., Skarina, T., Koteva, K., Guarne, A., Savchenko, A. and Wright, G.D. Rifampin phosphotransferase is an unusual antibiotic resistance kinase. Nat Commun 7 (2016) 11343. [PMID: 27103605]

[EC 2.7.9.6 created 2018]


Continued with EC 2.7.10 to EC 2.7.99
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